ID   GALT6_MOUSE             Reviewed;         622 AA.
AC   Q8C7U7; Q0VE84; Q3TWF0; Q8CED2; Q9QZ16;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 6;
DE            EC=2.4.1.41 {ECO:0000250|UniProtKB:Q8NCL4};
DE   AltName: Full=Polypeptide GalNAc transferase 6;
DE            Short=GalNAc-T6;
DE            Short=pp-GaNTase 6;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
GN   Name=Galnt6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric carcinoma;
RX   PubMed=10464263; DOI=10.1074/jbc.274.36.25362;
RA   Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N.,
RA   Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.;
RT   "Cloning and characterization of a close homologue of human UDP-N-
RT   acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3,
RT   designated GalNAc-T6. Evidence for genetic but not functional redundancy.";
RL   J. Biol. Chem. 274:25362-25370(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC       biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC       serine or threonine residue on the protein receptor. May participate in
CC       synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2,
CC       EA2 and fibronectin peptides (By similarity).
CC       {ECO:0000250|UniProtKB:Q8NCL4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC         [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC         Evidence={ECO:0000250|UniProtKB:Q8NCL4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC         O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC         Evidence={ECO:0000250|UniProtKB:Q8NCL4};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q14435};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q14435}.
CC   -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC       region: the N-terminal domain (domain A, also called GT1 motif), which
CC       is probably involved in manganese coordination and substrate binding
CC       and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC       which is probably involved in catalytic reaction and UDP-Gal binding.
CC       {ECO:0000250|UniProtKB:O08912}.
CC   -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC       to the glycopeptide specificity. {ECO:0000250|UniProtKB:Q8N4A0}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB55352.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Polypeptide N-acetylgalactosaminyltransferase 6;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_515";
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DR   EMBL; AJ133523; CAB55352.1; ALT_FRAME; mRNA.
DR   EMBL; AK028506; BAC25984.1; -; mRNA.
DR   EMBL; AK049222; BAC33618.1; -; mRNA.
DR   EMBL; AK155008; BAE32989.1; -; mRNA.
DR   EMBL; AK159721; BAE35316.1; -; mRNA.
DR   EMBL; BC119324; AAI19325.1; -; mRNA.
DR   EMBL; BC119326; AAI19327.1; -; mRNA.
DR   CCDS; CCDS27843.1; -.
DR   RefSeq; NP_001155239.1; NM_001161767.1.
DR   RefSeq; NP_001155240.1; NM_001161768.1.
DR   RefSeq; NP_766039.2; NM_172451.3.
DR   AlphaFoldDB; Q8C7U7; -.
DR   SMR; Q8C7U7; -.
DR   STRING; 10090.ENSMUSP00000056705; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q8C7U7; 2 sites, No reported glycans.
DR   GlyGen; Q8C7U7; 2 sites.
DR   PhosphoSitePlus; Q8C7U7; -.
DR   EPD; Q8C7U7; -.
DR   MaxQB; Q8C7U7; -.
DR   PaxDb; 10090-ENSMUSP00000056705; -.
DR   PeptideAtlas; Q8C7U7; -.
DR   ProteomicsDB; 267554; -.
DR   Antibodypedia; 14380; 221 antibodies from 22 providers.
DR   DNASU; 207839; -.
DR   Ensembl; ENSMUST00000052069.12; ENSMUSP00000056705.6; ENSMUSG00000037280.13.
DR   Ensembl; ENSMUST00000159715.8; ENSMUSP00000123848.2; ENSMUSG00000037280.13.
DR   Ensembl; ENSMUST00000161514.2; ENSMUSP00000124793.2; ENSMUSG00000037280.13.
DR   GeneID; 207839; -.
DR   KEGG; mmu:207839; -.
DR   UCSC; uc007xrz.2; mouse.
DR   AGR; MGI:1891640; -.
DR   CTD; 11226; -.
DR   MGI; MGI:1891640; Galnt6.
DR   VEuPathDB; HostDB:ENSMUSG00000037280; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000160845; -.
DR   HOGENOM; CLU_013477_0_3_1; -.
DR   InParanoid; Q8C7U7; -.
DR   OMA; SWFLHNI; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q8C7U7; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 207839; 7 hits in 80 CRISPR screens.
DR   PRO; PR:Q8C7U7; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8C7U7; Protein.
DR   Bgee; ENSMUSG00000037280; Expressed in molar tooth and 114 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISS:UniProtKB.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR045885; GalNAc-T.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF58; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 6; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   Genevisible; Q8C7U7; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW   Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..622
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 6"
FT                   /id="PRO_0000059115"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..622
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          506..622
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          176..285
FT                   /note="Catalytic subdomain A"
FT   REGION          348..410
FT                   /note="Catalytic subdomain B"
FT   BINDING         269
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         271
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         407
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         511
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         514
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         528
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   BINDING         533
FT                   /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT                   /ligand_id="ChEBI:CHEBI:67138"
FT                   /evidence="ECO:0000250|UniProtKB:H0ZAB5"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        509..527
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        553..566
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        597..610
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   CONFLICT        14
FT                   /note="A -> T (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="K -> R (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="K -> N (in Ref. 2; BAC25984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="V -> M (in Ref. 2; BAC25984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="K -> G (in Ref. 2; BAC25984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263..275
FT                   /note="EVLTFLDAHCECF -> KGAHVSWTPTVSVS (in Ref. 1;
FT                   CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="A -> P (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="E -> Q (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="E -> G (in Ref. 2; BAC25984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="R -> Q (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="G -> S (in Ref. 1; CAB55352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   622 AA;  71537 MW;  6DBCA3A2CCFDBDAA CRC64;
     MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK DQVLDFMLGA
     VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK PFWDRPPQDP NSPGADGKAF
     QKKEWTNLET KEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLPTTS
     VIIVFHNEAW STLLRTVYSV LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV
     VRQRERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT
     IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK SPTFAGGLFS
     ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
     TSVIARNQVR LAEVWMDDYK KIFYRRNLQA AKMVQENNFG DISERLRLRE QLRCHNFSWY
     LHNVYPEMFV PDLNPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS
     QRDLRHNIGK QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS
     QDKKPAMAPC NPRDPYQLWL FV
//